1i1c
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(New page: 200px<br /><applet load="1i1c" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i1c, resolution 2.70Å" /> '''NON-FCRN BINDING FC ...)
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Revision as of 14:51, 20 November 2007
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NON-FCRN BINDING FC FRAGMENT OF RAT IGG2A
Overview
The neonatal Fc receptor (FcRn) transports immunoglobulin G (IgG) across, epithelia, binding IgG in acidic vesicles (pH < or = 6.5) and releasing, IgG in the blood at pH 7.4. Well-ordered FcRn/Fc crystals are prevented by, the formation of "oligomeric ribbons" of FcRn dimers bridged by Fc, homodimers, thus we crystallized a 1:1 complex between rat FcRn and a, heterodimeric Fc containing only one FcRn binding site. The 2.8 A complex, structure demonstrates that FcRn uses its alpha2 and beta2-microglobulin, domains and carbohydrate to interact with the Fc C(gamma)2-C(gamma)3, interface. The structure reveals conformational changes in Fc and three, titratable salt bridges that confer pH-dependent binding, and can be used, to guide rational design of therapeutic IgGs with longer serum half-lives.
About this Structure
1I1C is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding., Martin WL, West AP Jr, Gan L, Bjorkman PJ, Mol Cell. 2001 Apr;7(4):867-77. PMID:11336709
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